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Solution structure of the Ras binding domain of the protein kinase Byr2 from Schizosaccharomyces pombe

Gronwald, W., Huber, F., Grünewald, P., Spörner, M., Wohlgemuth, S., Herrmann, C. and Kalbitzer, Hans Robert (2001) Solution structure of the Ras binding domain of the protein kinase Byr2 from Schizosaccharomyces pombe. Structure 9 (11), pp. 1029-1041.

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BACKGROUND: After activation, small GTPases such as Ras transfer the incoming signal to effectors by specifically interacting with the binding domain of these proteins. Structural details of the binding domain of different effectors determine which pathway is predominantly activated. Byr2 from fission yeast is a functional homolog of Raf, which is the direct downstream target of Ras in mammalians ...


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Item type:Article
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
11709167PubMed ID
Amino Acid SequenceMESH
Binding SitesMESH
Enzyme ActivationMESH
Fungal Proteins/metabolismMESH
Guanylyl Imidodiphosphate/chemistryMESH
MAP Kinase Kinase KinasesMESH
Mitogen-Activated Protein Kinases/metabolismMESH
Models, MolecularMESH
Molecular Sequence DataMESH
Nuclear Magnetic Resonance, BiomolecularMESH
Protein BindingMESH
Protein Structure, SecondaryMESH
Protein Structure, TertiaryMESH
Schizosaccharomyces pombe ProteinsMESH
Sequence Homology, Amino AcidMESH
ras Proteins/metabolismMESH
Dewey Decimal Classification:500 Science > 570 Life sciences
Created at the University of Regensburg:Unknown
Item ID:16579
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